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Genetic heterogeneity of membrane‐bound β‐glucosidase in Gaucher's disease
Author(s) -
Carroll M.
Publication year - 1981
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf02263575
Subject(s) - thermostability , enzyme , heterozygote advantage , biochemistry , membrane , chemistry , biology , genotype , gene
Membrane‐bound β‐glucosidase of leukocytes exists in two forms, one with optimal activity at about pH 4.5, whereas the other is most active at pH 5.5–6.0. In one case of type 1 (adult) Gaucher's disease, the pH 4.5 activity was totally deficient, but the pH 5.5 activity was present in normal amounts; obligate heterozygotes had half the normal activity at pH 4.5. In two different cases, the membrane‐bound β‐glucosidase was completely absent when assayed at either pH 4.5 or pH 5.5. Two further cases had residual activity at both pH values; however, the residual enzymes had different thermostability properties than the corresponding enzymes of control leukocytes. The results are consistent with the existence of at least three genetic variants of type 1 (adult) Gaucher's disease.